(S)-2-[3-(11-tert-Butoxycarbonylamino-1,5-dioxa-spiro[5.5]undec-7-yl)-propionylamino]-3-phenyl-propionic acid methyl ester | 248260-52-8

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羧酸及其衍生物
• 英文名称: (S)-2-[3-(11-tert-Butoxycarbonylamino-1,5-dioxa-spiro[5.5]undec-7-yl)-propionylamino]-3-phenyl-propionic acid methyl ester
• CAS: 248260-52-8
• 化学式: C₂₇H₄₀N₂O₇
• 分子量: 504.624
• InChiKey: ISGYDCWNWANEOB-ORFBVSJDSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.49
• 重原子数：
  36.0
• 可旋转键数：
  8.0
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.67
• 拓扑面积：
  112.19
• 氢给体数：
  2.0
• 氢受体数：
  7.0

反应信息

• 作为反应物：
  描述：

  (S)-2-[3-(11-tert-Butoxycarbonylamino-1,5-dioxa-spiro[5.5]undec-7-yl)-propionylamino]-3-phenyl-propionic acid methyl ester 在 三异丙基硅烷 、 O-(1H-benzotriazol-1-yl)-N,N,N',N'-tetramethyluronium hexafluorophosphate 、 N,N-二异丙基乙胺 、 三氟乙酸 作用下， 以 二氯甲烷 、 N,N-二甲基甲酰胺 为溶剂， 反应 1.0h， 生成
  参考文献：
  名称：

  Combinatorial Library of Serine and Cysteine Protease Inhibitors That Interact with Both the S and S‘ Binding Sites

  摘要：

  A combinatorial library of 400 inhibitors has been synthesized and screened against several serine and cysteine proteases including plasmin, cathepsin B, and papain. The inhibitors are based upon a cyclohexanone nucleus and are designed to probe binding interactions in the S2 and S2' binding sites. This methodology has led to the discovery of inhibitor 15A, which incorporates Trp at both the P2 and P2' positions and has an inhibition constant against plasmin of 5 mu M. Data from screening of the library shows that plasmin has a strong specificity for Trp at the S2 subsite and prefers to bind hydrophobic and aromatic amino acids such as Ile, Phe, Trp, and Tyr at the S2' subsite. In contrast, the S2' subsites of cathepsin B and papain do not show a strong preference for any particular amino acid.

  DOI：

  10.1021/jm990272g
• 作为产物：
  描述：

  L-苯丙氨酸甲酯 、 在 O-(1H-benzotriazol-1-yl)-N,N,N',N'-tetramethyluronium hexafluorophosphate 、 N,N-二异丙基乙胺 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 3.0h， 以74%的产率得到(S)-2-[3-(11-tert-Butoxycarbonylamino-1,5-dioxa-spiro[5.5]undec-7-yl)-propionylamino]-3-phenyl-propionic acid methyl ester
  参考文献：
  名称：

  Combinatorial Library of Serine and Cysteine Protease Inhibitors That Interact with Both the S and S‘ Binding Sites

  摘要：

  A combinatorial library of 400 inhibitors has been synthesized and screened against several serine and cysteine proteases including plasmin, cathepsin B, and papain. The inhibitors are based upon a cyclohexanone nucleus and are designed to probe binding interactions in the S2 and S2' binding sites. This methodology has led to the discovery of inhibitor 15A, which incorporates Trp at both the P2 and P2' positions and has an inhibition constant against plasmin of 5 mu M. Data from screening of the library shows that plasmin has a strong specificity for Trp at the S2 subsite and prefers to bind hydrophobic and aromatic amino acids such as Ile, Phe, Trp, and Tyr at the S2' subsite. In contrast, the S2' subsites of cathepsin B and papain do not show a strong preference for any particular amino acid.

  DOI：

  10.1021/jm990272g